{"id":"773c1cd4-d8fe-57c8-b61a-e8ad2c681bf6","stable_key":"d17caac5-7018-5ca8-9e96-95afeb384bc4:pectin-rgii-a","predicate":"catalyzes","statement":"BT0996 contains a beta-D-glucuronidase module targeting RG-II chain A.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"48a8e5f8-e04c-5430-a7c1-94690cd02c8c","mechanism_event_label":"A two-part bacterial protein removes one decoration from complex RG-II.","subject":{"id":"4752c90d-626d-5e00-86eb-f6474de2d428","slug":"bt-bt0996","display_name":"Bacteroides thetaiotaomicron BT0996, dual RG-II glycosidase","entity_type_key":"protein"},"object":{"id":"34e8d447-8351-59af-8504-395fc3cecbb4","slug":"bt-rgii-chain-a-cleavage","display_name":"B. thetaiotaomicron RG-II chain-A glucuronide cleavage","entity_type_key":"cellular_process"},"evidence_count":1,"mechanism_event":{"id":"48a8e5f8-e04c-5430-a7c1-94690cd02c8c","stable_key":"d17caac5-7018-5ca8-9e96-95afeb384bc4:pectin-rgii-a-event","event_type":"biochemical_relationship","label":"A two-part bacterial protein removes one decoration from complex RG-II.","description":"BT0996 contains a beta-D-glucuronidase module targeting RG-II chain A.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"ef09fcc7-de79-5e63-b329-8a148639469e","slug":"pectic-rhamnogalacturonan-ii","display_name":"Pectic rhamnogalacturonan II / RG-II","entity_type_key":"chemical_species"},"role":"substrate","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"4752c90d-626d-5e00-86eb-f6474de2d428","slug":"bt-bt0996","display_name":"Bacteroides thetaiotaomicron BT0996, dual RG-II glycosidase","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"34e8d447-8351-59af-8504-395fc3cecbb4","slug":"bt-rgii-chain-a-cleavage","display_name":"B. thetaiotaomicron RG-II chain-A glucuronide cleavage","entity_type_key":"cellular_process"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""}]},"contexts":[{"dimension":"evidence_span","value_text":"{\"source_cache\": \"artifacts/pectin-research/28329766.fulltext.txt\", \"locator\": \"Primary full-text span; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"e0298d5bf6cef49e211cd0230c691566f2a68a0b7c6642040c50687ac8dcd55f\", \"start_char\": 3702, \"end_char\": 4301, \"text_sha256\": \"b0577db49fd5f5b6c8a42a003ad49148b31012228ed996430885de1d4fbd6fe0\"}","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Recombinant enzyme dissection and structures","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"Purified plant RG-II and defined enzymatic substrates","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"The linked corrigendum DOI 10.1038/nature23659 corrects attribution of glycan symbols to SNFG; it does not reverse these enzyme results. 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This is microbial biochemistry.\nexposure: Purified plant RG-II and defined enzymatic substrates\nevidence_span: {\"source_cache\": \"artifacts/pectin-research/28329766.fulltext.txt\", \"locator\": \"Primary full-text span; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"e0298d5bf6cef49e211cd0230c691566f2a68a0b7c6642040c50687ac8dcd55f\", \"start_char\": 3702, \"end_char\": 4301, \"text_sha256\": \"b0577db49fd5f5b6c8a42a003ad49148b31012228ed996430885de1d4fbd6fe0\"}\n[pectin-p28329766] Complex pectin metabolism by gut bacteria reveals novel catalytic functions. (2017). https://pubmed.ncbi.nlm.nih.gov/28329766/ DOI: 10.1038/nature21725","model_system":"Recombinant enzyme dissection and structures","directness":"author_interpretation","verification_status":"source_derived_draft","notes":"Exact curation-document quotation, not publisher quotation. Study references: [pectin-p28329766] Complex pectin metabolism by gut bacteria reveals novel catalytic functions. 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